Linked Life Data

16697972

Source:http://linkedlifedata.com/resource/pubmed/id/16697972

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5-6
pubmed:dateCreated
2006-7-10
pubmed:abstractText
The peripheral stalk of F-ATPases is an essential component of these enzymes. It extends from the membrane distal point of the F1 catalytic domain along the surface of the F1 domain with subunit a in the membrane domain. Then, it reaches down some 45 A to the membrane surface, and traverses the membrane, where it is associated with the a-subunit. Its role is to act as a stator to hold the catalytic alpha3beta3 subcomplex and the a-subunit static relative to the rotary element of the enzyme, which consists of the c-ring in the membrane and the attached central stalk. The central stalk extends up about 45 A from the membrane surface and then penetrates into the alpha3beta3 subcomplex along its central axis. The mitochondrial peripheral stalk is an assembly of single copies of the oligomycin sensitivity conferral protein (the OSCP) and subunits b, d and F6. In the F-ATPase in Escherichia coli, its composition is simpler, and it consists of a single copy of the delta-subunit with two copies of subunit b. In some bacteria and in chloroplasts, the two copies of subunit b are replaced by single copies of the related proteins b and b' (known as subunits I and II in chloroplasts). As summarized in this review, considerable progress has been made towards establishing the structure and biophysical properties of the peripheral stalk in both the mitochondrial and bacterial enzymes. However, key issues are unresolved, and so our understanding of the role of the peripheral stalk and the mechanism of synthesis of ATP are incomplete.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:volume
1757
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
286-96
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
The peripheral stalk of the mitochondrial ATP synthase.
pubmed:affiliation
The Medical Research Council Dunn Human Nutrition Unit, The Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 2XY, UK. walker@mrc-dunn.cam.ac.uk
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't